ArticleJournal of bacteriology2005
The metalloprotease of Listeria monocytogenes controls cell wall translocation of the broad-range phospholipase C.
Article in Journal of bacteriology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
20 citing papers in PubMed, 50 citations in OpenAlex.
- Structural basis for the unique molecular properties of broad-range phospholipase C from Listeria monocytogenes.Nature communications · 2023Article
- Transcriptome Analysis of Listeria monocytogenes Exposed to Beef Fat Reveals Antimicrobial and Pathogenicity Attenuation Mechanisms.Applied and environmental microbiology · 2021Article
- Review
- A Cross-Protective Vaccine Against 4b and 1/2bFrontiers in microbiology · 2020Article
- The Metalloprotease Mpl Supports Listeria monocytogenes Dissemination through Resolution of Membrane Protrusions into Vacuoles.Infection and immunity · 2016Article
- Recombinant broad-range phospholipase C from Listeria monocytogenes exhibits optimal activity at acidic pH.Biochimica et biophysica acta · 2016Article
- A non-catalytic histidine residue influences the function of the metalloprotease of Listeria monocytogenes.Microbiology (Reading, England) · 2014Article
- Membrane chaperone SecDF plays a role in the secretion of Listeria monocytogenes major virulence factors.Journal of bacteriology · 2013Article
- Protein transport across the cell wall of monoderm Gram-positive bacteria.Molecular microbiology · 2012Review
- Posttranslocation chaperone PrsA2 regulates the maturation and secretion of Listeria monocytogenes proprotein virulence factors.Journal of bacteriology · 2011Article
- The metalloprotease of Listeria monocytogenes is regulated by pH.Journal of bacteriology · 2011Article
- Functional analysis of the Listeria monocytogenes secretion chaperone PrsA2 and its multiple contributions to bacterial virulence.Molecular microbiology · 2011Article
- Differentiation of propeptide residues regulating the compartmentalization, maturation and activity of the broad-range phospholipase C of Listeria monocytogenes.The Biochemical journal · 2010Article
- Listeria monocytogenes PrsA2 is required for virulence factor secretion and bacterial viability within the host cell cytosol.Infection and immunity · 2010Article
- The posttranslocation chaperone PrsA2 contributes to multiple facets of Listeria monocytogenes pathogenesis.Infection and immunity · 2009Article
- The propeptide of the metalloprotease of Listeria monocytogenes controls compartmentalization of the zymogen during intracellular infection.Journal of bacteriology · 2009Article
- Development of a mariner-based transposon and identification of Listeria monocytogenes determinants, including the peptidyl-prolyl isomerase PrsA2, that contribute to its hemolytic phenotype.Journal of bacteriology · 2009Article
- Listeria monocytogenes phosphatidylinositol-specific phospholipase C: Kinetic activation and homing in on different interfaces.Biochemistry · 2009Article
- The metalloprotease of Listeria monocytogenes is activated by intramolecular autocatalysis.Journal of bacteriology · 2008Article
- Compartmentalization of the broad-range phospholipase C activity to the spreading vacuole is critical for Listeria monocytogenes virulence.Infection and immunity · 2007Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Listeria monocytogenes is a gram-positive bacterial pathogen that multiplies in the cytosol of host cells and spreads directly from cell to cell. During cell-to-cell spread, bacteria become temporarily confined to secondary vacuoles. The broad-range phospholipase C (PC-PLC) of L. monocytogenes contributes to bacterial escape from secondary vacuoles. PC-PLC requires cleavage of an N-terminal propeptide for activation, and Mpl, a metalloprotease of Listeria, is involved in the proteolytic activation of PC-PLC. Previously, we showed that cell wall translocation of PC-PLC is inefficient, resulting in accumulation of PC-PLC at the membrane-cell wall interface. In infected cells, rapid cell wall translocation of PC-PLC is triggered by a decrease in pH and correlates with cleavage of the propeptide in an Mpl-dependent manner. To address the role of the propeptide and of Mpl in cell wall translocation of PC-PLC, we generated a cleavage site mutant and a propeptide deletion mutant. The intracellular behavior of these mutants was assessed in pulse-chase experiments. We observed efficient translocation of the proform of the PC-PLC cleavage site mutant in a manner that was pH sensitive and Mpl dependent. However, the propeptide deletion mutant was efficiently translocated into host cells independent of Mpl and pH. Overall, these results suggest that Mpl regulates PC-PLC translocation across the bacterial cell wall in a manner that is dependent on the presence of the propeptide but independent of propeptide cleavage. In addition, similarly to Mpl-mediated cleavage of PC-PLC propeptide, Mpl-mediated translocation of PC-PLC across the bacterial cell wall is pH sensitive.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.